Principles of Ubiquitin-Dependent Signaling

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing

Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944

The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy

Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125

Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain

Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872

Gastric Cancer Secreted miR-214-3p Inhibits the Anti-Angiogenesis Effect of Apatinib by Suppressing Ferroptosis in Vascular Endothelial Cells.Preprint

Ba, Y., wang, T., Yang, C., Wang, W., Zhang, Y., Zhu, Q., & Zhang, H. (2022) · Research Square · doi:10.21203/rs.3.rs-1963577/v1

Epigenetic aspects of a putative mechanism of antitumor action of ferrocenylalkylazoles

Babin, V. N., Belousov, Y. А., & Kulikov, V. N. (2024) · Russian Chemical Bulletin · doi:10.1007/s11172-024-4397-1

Neddylation inhibition affects cell proliferation and steroidogenesis in sheep follicular granulosa cells

Lyu, L., Qin, X., Xiu, H., Qu, Y., Wang, Y., Yang, X., Dang, W., & Kebreab, E. (2025) · Theriogenology · doi:10.1016/j.theriogenology.2025.02.020

Emerging Concept of Receptor Endocytosis and Signaling

Kumar, A., Panda, A., Kumar, S., & Ranjan, K. (2025) · The Receptors · doi:10.1007/978-3-031-81991-9_3

Unique Gluing Effect of ASXL1 K351 Monoubiquitination Stimulates PR-DUB-Mediated Nucleosomal H2AK119Ub DeubiquitinationPreprint

Zhang, T., Zheng, J., Tong, Z., Deng, Z., He, Z., Wu, X., Wang, M., Du, Y., Xu, Z., Tao, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.25.650627

Covalent inhibition of Plasmodium falciparum Ubc13 impairs global protein synthesis

Truong, A., Hu, R., Quan, B., Bailey, M. A., Schroeder, E. A., Sylvester, K., Neveu, G., Kafsack, B. F. C., Fitzgerald, M. C., & Derbyshire, E. R. (2025) · iScience · doi:10.1016/j.isci.2025.112545 · Cited by 1

Prognostic Value of Ubiquitination‐Related Genes in Ovarian Cancer and Their Correlation With Tumor Immunity

Zhao, S., Lin, X., Huang, Y., Kang, Z., Luo, H., Zhang, Q., Li, Q., & Li, M. (2025) · Human Mutation · doi:10.1155/humu/8369299

Site-Specific Nanobody Inhibitors of the Proteasomal Deubiquitinase UCH37Preprint

Li, Y., Chang, L. H., Patel, R. S., Shestoperova, E. I., Du, J., Salam, M., Doig, A. N. R., Das, C., & Strieter, E. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.11.669711

Unraveling the mechanisms of ubiquitin-specific proteases in hepatocellular carcinoma: A focus on inhibitors

Xu, Y., & Ye, J. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109049 · Cited by 1

Decoding VEXAS syndrome: emerging insights into pathogenesis and clinical management

Fiumara, M., Campochiaro, C., & Molteni, R. (2025) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000001137

Bioinformatics Analysis of Gene Expression in PCOS, Ovarian Cancer and Recurrent Pregnancy Loss

Vasa, S., Shibu, S., Samantaray, S., Kaloni, A., Joshi, N., Parekh, B., & Modi, A. (2025) · Current Genetic Medicine Reports · doi:10.1007/s40142-025-00231-4

The role of ubiquitination in the pathogenesis of atrial fibrillation: mechanisms and therapeutic implications

Runtian, Z., Xing, G., You, S., Zimeng, S., Wenqiang, H., Cui, L., Qingrun, M., & Jingquan, Z. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1784147

CEP55's developmental MARCH : from structural biology of its Ubiquitin-Binding Domains to precision medicine through phenotypic screening of terminal cytokinesis

Boullé, M. (2021) · theses.fr (ABES) · doi:10.70675/0a20ec5cz222ez4b70za5e2z54dffe8e7e65

Regulation of NFATc3 stability by SUMO and E3 ubiquitin-ligases Trim39 and Trim17

Basu-Shrivastava, M. (2020) · theses.fr (ABES) · doi:10.70675/0aa33054zc607z413dz8aedz05ed052d5438 · Cited by 1

Sumo-Directed Control of the Resolvase Yen1 in Mitotic Cells

Dorison, H. (2021) · theses.fr (ABES) · doi:10.70675/c6e7956fzf5a7z4302zb2e4z1d7be2f97f64

Hypertonicity-induced RNF183 targets NKCC1 to protect kidney collecting duct cells but induces apoptosis in colon cells

Okamoto, T., Higashi, Y., Takemoto, M., Matsuhisa, K., Sato, S., Saito, A., Omura, I., Kamikawa, Y. F., Imaizumi, K., & Kaneko, M. (2026) · Communications Biology · doi:10.1038/s42003-026-09766-w

Protein structural dynamics in bacteria via nitroxide-based SDSL-EPR spectroscopy : from method improvements to in-cell studies

Pierro, A. (2021) · doi:10.70675/39f8a77cz8a4fz4b03za3ccz3de625c18f55

Functional analysis of the nonconventional myosin myosin1g in zebrafish left-right asymmetry

Kurup, A. J. (2022) · theses.fr (ABES) · doi:10.70675/0c93f514z3fc7z409ezaed7z5751e5abf7ab

Identification of E3 ligase substrates and PROTAC-induced ubiquitylation sites using proximity-based identification of ubiquitin sites (PrIUS)

Tessier, T. M., Maitland, M. E. R., Kutera, M., Dybas, J. M., St‐Germain, J. R., Arrowsmith, C. H., Baršytė-Lovejoy, D., Zhang, W., Raught, B., & Weitzman, M. D. (2026) · Communications Biology · doi:10.1038/s42003-026-09964-6

The potato ubiquitin carboxyl-terminal hydrolase StUCH1 positively regulates drought tolerance by enhancing antioxidant defense capacityPreprint

Shang, M., Ghimire, S., Poudel, B., Kharel, R., Fu, X., Zhang, H., & Tang, X. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6551821

The E3 ubiquitin ligase UBR5 promotes ubiquitylation and degradation of the chromatin regulator ATAD2

Honda, R., Takao, M., Akizuki, Y., & Ohtake, F. (2026) · FEBS Letters · doi:10.1002/1873-3468.70339

GIPC2 suppresses colorectal cancer progression via regulation by UBA1-mediated ubiquitination

Cui, X., Chen, Y., Rao, Q., Zhang, Q., Zhang, Y., Ning, S., & Zhang, Z. (2026) · Gastroenterology report · doi:10.1093/gastro/goag057

Proteome-wide Ubiquitinome Profiling Reveals Substrate-specific Dynamics Within the USP7 Network

van der Meer, J. W., van der Knaap, J. A., Sijm, A., Bezstarosti, K., Dekkers, D. H. W., Doff, W. A. S., Demmers, J., & Verrijzer, C. P. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101602

Systemic degradation of repressive transcription factors gates gene expression and cell fate specificationPreprint

Jevtić, P., Witus, S. R., McCloud, D. M., Yang, Z., Milunovic-Jevtic, A., Roh, H., & Rapé, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.16.732780

Role of E3 Ubiquitin Ligases in Oligodendrocyte Health and Disease

Mabb, A. M., Pyaram, D. N., & Samanta, J. (2026) · ASN NEURO · doi:10.1080/17590914.2026.2682220

SUMOylation of HSF1 orchestrates transcriptional and splicing programs during the proteotoxic stress responsePreprint

Müller, S. P., Patra, U., Kuska, S., Mosler, T., Makarov, T., Mukhopadhyay, U., Münch, C., Keller, U. B., Müller-McNicoll, M., & Wirth, M. (2026) · Research Square · doi:10.21203/rs.3.rs-10283915/v1

Efficient and Controllable Assembly of Multitype Polyubiquitin Chains via Enzyme-Assisted Thiol Ligation for Structural Elucidation

Pan, B.-B., Zhou, C., Yang, Y., Zhang, X., Cui, C., Li, Y., & Su, X. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c04268

The role of E3 ubiquitin ligases in selective types of macroautophagy

Müller, M., Winklhofer, K. F., & Reggiori, F. (2026) · EMBO Reports · doi:10.1038/s44319-026-00887-1

Neddylation cooperates with multiple phosphorylation to enhance FGFR1 stability and drive breast cancer progression

Du, Y., Ning, D., Yu, J., Chen, Y., Li, J., Liu, C., Lin, C., Zhang, T., Liu, W., Qin, J., et al. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.115141

Polygenic burden of ubiquitin system genes in schizophrenia: focus on prenatal neurodevelopmentPreprint

Alacid, G. R., Guardiola-Ripoll, M., Almodóvar-Payá, C., Herrera-Escartín, D., Hostalet, N., Rodríguez‐Cano, E., Salvador, R. M., Sarró, S., Guerrero‐Pedraza, A., Salavert, J., et al. (2026) · medRxiv · doi:10.64898/2026.07.28.26359147

Synthesis of Linkage-Specific Polyubiquitin Probes Using Unnatural Amino Acids

Buhl, M. T., & Cropp, T. A. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5112-4_3

FAF1 cofactor enhances UFD1/NPL4-p97 unfolding efficiency across ubiquitin chain lengths independent of SUMO2Preprint

Lemmon, A. A., & Lima, C. D. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.31.742138

Genome-Wide Characterization and Transcriptomic Analysis Reveal Light-Quality-Responsive RING Zinc Finger Genes in Potatoes

Pan, P., Guo, R., Sa, G., Yang, H., Cheng, L., Yuan, J., Liu, J., & Yu, B. (2026) · Plants · doi:10.3390/plants15192915

Systemic energy and neuroinflammatory disturbances in a lactacystin-induced rat model of Parkinson's disease

Khunderyakova, N. V., Pshenichnikova, T. V., Malkov, A., Булгин, И. В., Khmil, N. V., Medvedeva, V. P., Glushkova, O. V., Lunin, S. M., Parfenyuk, S. B., Khrenov, M. O., et al. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.116035

Editorial: E3 ubiquitin ligases: critical roles in cancer progression and therapeutic implications

Koganti, P., & Liu, P. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1995835

Ubiquitin E3 ligases in atherosclerosis: mechanisms of vascular cell plasticity and opportunities for targeted protein degradation

Sun, X., Zoni, R. N., Tanni, F. Y., Khalimonchuk, M., & Huabo, S. (2026) · Current Opinion in Physiology · doi:10.1016/j.cophys.2026.101000

Epigenetic regulatory networks in the pathogenesis and treatment of osteoporosis subtypes

Ren, Z., Dai, B., Chen, D., Li, Z., Meng, K., Lan, S., Liu, C., 张忠民, & Hao, J. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00630-1

BindingDB Entry 50019176: Inhibition of the Ubiquitin Transfer Cascade by a Peptidomimetic Foldamer Mimicking the E2 N-Terminal Helix.

BindingDB (2024) · UC San Diego · doi:10.7270/q2d79grt

BindingDB Entry 50019232: Development of Human Carbonic Anhydrase II Heterobifunctional Degraders.

BindingDB (2024) · UC San Diego · doi:10.7270/q2gx4gxp

FAIRsharing record for: BioGRID Open Repository of CRISPR Screens

FAIRsharing Team (2018) · FAIRsharing.org · doi:10.25504/fairsharing.lkaome

The ubiquitination code: a signalling problem

Woelk, T., Sigismund, S., Penengo, L., & Polo, S. (2007) · Cell Division · doi:10.1186/1747-1028-2-11 · Cited by 152

The increasing complexity of the ubiquitin code

Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054

Post-translational regulation of ubiquitin signaling

Song, L., & Luo, Z. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902074 · Cited by 345

E3 Ligase-Mediated Protein Quality Control Mechanisms: Insights into Maintaining Cellular Integrity Across Pluripotency, Cancer, and Neurodegeneration

Kolla, S. (2024) · eScholarship (California Digital Library)

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 621